Effect of CNT on collagen fiber structure, stiffness assembly kinetics and stem cell differentiation.
Effect of CNT on collagen fiber structure, stiffness assembly kinetics and stem cell differentiation.
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DOI：
10.1016/j.msec.2015.01.014
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发表时间：
2015-04
期刊：
影响因子：
--
通讯作者：
Wang R
中科院分区：
文献类型：
--
作者：
Kim T;Sridharan I;Zhu B;Orgel J;Wang R
胶原蛋白是一种天然的一维纳米材料。碳纳米管（CNT）被发现与生物材料的接口，并显示出良好的应用前景，在创建组织工程和再生医学的增强支架。在这项研究中，我们研究了CNT在胶原纤维结构，机械强度和组装动力学中的独特作用。结果表明，CNT与胶原蛋白在分子水平上相互作用。它使胶原纤维的螺旋线圈松弛，并具有使纤维变平的作用，从而导致D-周期延长，这是胶原纤维的特征性条带特征。氧化的CNT的表面电荷导致在胶原原纤维形成期间增强的局部离子强度，解释胶原-CNT（COL-CNT）纤维组装的较慢动力学和较厚纤维的形成。由于CNT的刚性，CNT的添加显著增加了纤维刚度。当作为基质用于人壁蜕膜胎盘干细胞（hdpPSC）分化时，发现COL-CNT支持归因于延长的D期的快速且有效的神经分化。这些结果突出了CNT在分子水平上调节胶原纤维组装的优越性。该研究还证实了使用CNT来增强胶原蛋白的生物和生物医学应用功能。
Collagen is a native one-dimensional nanomaterial. Carbon nanotube (CNT) was found to interface with biological materials and show promising applications in creating reinforced scaffolds for tissue engineering and regenerative medicine. In this study, we examined the unique role of CNT in collagen fiber structure, mechanical strength and assembly kinetics. The results imply that CNT interacts with collagen at the molecular level. It relaxes the helical coil of collagen fibrils and has the effect of flattening the fibers leading to the elongation of D-period, the characteristic banding feature of collagen fibers. The surface charge of oxidized CNT leads to enhanced local ionic strength during collagen fibrilogenesis, accounting for the slower kinetics of collagen-CNT (COL-CNT) fiber assembly and the formation of thicker fibers. Due to the rigidity of CNT, the addition of CNT increases the fiber stiffness significantly. When applied as a matrix for human decidua parietalis placental stem cells (hdpPSCs) differentiation, COL-CNT was found to support fast and efficient neural differentiation ascribed to the elongated D-period. These results highlight the superiority of CNT to modulate collagen fiber assembly at the molecular level. The study also exemplifies the use of CNT to enhance the functionality of collagen for biological and biomedical applications.
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